ID G1QGF0_MYOLU Unreviewed; 529 AA.
AC G1QGF0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 3 {ECO:0000313|Ensembl:ENSMLUP00000022783.1};
GN Name=ENTPD3 {ECO:0000313|Ensembl:ENSMLUP00000022783.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022783.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000022783.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000022783.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; AAPE02039235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02039236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QGF0; -.
DR STRING; 59463.ENSMLUP00000022783; -.
DR Ensembl; ENSMLUT00000023063.1; ENSMLUP00000022783.1; ENSMLUG00000028733.1.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01100000263542; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; G1QGF0; -.
DR OMA; GNAISDM; -.
DR TreeFam; TF332859; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IEA:Ensembl.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:Ensembl.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF38; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 222..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 529 AA; 59053 MW; C60213F2149FC10E CRC64;
MLTVLTRQPC EHAGFKALSR TPVVVALVVL ILSVVVLVAI TLIQIHQKEV LLPGLKYGIV
LDAGSSRTTV YVYQWPAEKE NNTGVVTQTS RCSVKGSGIS SYGKNPQDAP KAFEDCMRKV
KEQIPAHLQG STHIYLGATA GMRLLRLQNE TAANEVLASI QNYFKSQPFD FRGAQIISGQ
EEGIYGWITA NYLMGNFLEK DLWHMWVHPN GVETTGALDL GGASTQISFA VGEKAELNTS
DIIKVSLYGY VYTLYTRSFQ CYGRNEAEKR FLAMLLQVPE NDSSPGIPCY PRNYSTTFTA
GHLFDSLCTE ELRPGGYDPD DTITFEGTGD PLLCRVKVAS LFAFRACHDR EICCFDGVYQ
PEVKGSFVAF AGFFYTANAL NLSGSFSLNA FNSSTWDFCS QDWSQLPLLL PRFDEVYARS
YCFSAHYIYH LLVSGYKFTE DTWPQIHFKK EVDNSSIAWS LGYMLTLTNQ IPAEIPLIRL
PMKPPTFMSV LAFFTGVALL CLGFLVYLYA LSRNQRRSQH ALDHAVDSE
//